Detection of Lectin Protein Allergen of Kidney Beans (Phaseolus vulgaris L.) and Desensitization Food Processing Technology

Abstract

With the increase of food allergy events related to not properly cooked kidney beans (Phaseolus vulgaris L.), more and more researchers are paying attention to the sensitization potential of lectin, one of the major storage and defensive proteins with the specific carbohydrate-binding activity. The immunoglobulin E (IgE), non-IgE, and mixed allergic reactions induced by the lectins were inducted in the current paper, and the detection methods of kidney bean lectin, including the purification strategies, hemagglutination activity, specific polysaccharide or glycoprotein interactions, antibody combinations, mass spectrometry methods, and allergomics strategies, were summarized, while various food processing aspects, such as the physical thermal processing, physical non-thermal processing, chemical modifications, and biological treatments, were reviewed in the potential of sensitization reduction. It might be the first comprehensive review on lectin allergen detection from kidney bean and the desensitization strategy in food processing and will provide a basis for food safety control.

Naturally Occurring Plant Food Toxicants and the Role of Food Processing Methods in Their Detoxification

“…Upon ingestion, legume lectins bind to particular receptor sites on the intestinal epithelial cell surface, interfering with nutrient absorption across the intestinal wall in a non-specific manner [ 131 , 141 ]. Once bound to the digestive tract, the lectin may alter part or all of the digestive, absorptive, protecting, and secretory functions of the entire digestive system, as well as cellular proliferation and turnover.…”

New Perspectives on Food Matrix Modulation of Food Allergies: Immunomodulation and Component Interactions

“…With the increase in food allergy events related to kidney beans, more and more researchers are paying attention to the allergenic potential of lectins in kidney beans. 51 Lectin is a nonenzymatic sugar-binding protein that can bind to specific monosaccharides and oligosaccharides to form complexes. 52 In addition, sensitization of kidney bean lectin proteins has also been reported in mice, pigs, cattle, etc., 53,54 whereas studies found that deglycation modification contributed to the reduction of soybean lectin allergen sensitivity, which also indicated the role of carbohydrates for lectin sensitization.…”

“…After covalent binding, allergenic epitopes can be modified or combined to lose allergenicity, and glycoproteins in animals and plants can be deglycated, which can lead to the destruction of allergenic epitopes (Figure C). With the increase in food allergy events related to kidney beans, more and more researchers are paying attention to the allergenic potential of lectins in kidney beans . Lectin is a nonenzymatic sugar-binding protein that can bind to specific monosaccharides and oligosaccharides to form complexes .…”

Pulse Protein Isolates as Competitive Food Ingredients: Origin, Composition, Functionalities, and the State-of-the-Art Manufacturing

“…Legumin is a hexameric protein with a stiff conformation and considerable quaternary structure, with a molecular mass of 300 to 400 kDa [ 9 , 51 ]. It is composed of six subunit pairs (each around 60 kDa), which interact noncovalently, and is further assembled through two trimeric intermediates ( Figure 2 A).…”